General Information
-
DRAMP ID
- DRAMP03280
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Peptide Name
- AcAMP (A. clavatus antimicrobial peptide)
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Source
- Aspergillus clavatus ES1
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Family
- Not found
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Gene
- Not found
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Sequence
- ATYDGKCYKKDNICKYKAQSGKTAICKCYVKVCPRDGAKCEFDSYKGKCYC
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Sequence Length
- 51
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UniProt Entry
- No entry found
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Protein Existence
- Not found
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiviral, Antifungal
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Target Organism
-
- Gram-positive bacteria: Staphylococcus aureus (MIC=20 µg/ml), Bacillus cereus (MIC=10 µg/ml), Micrococcus luteus (MIC=10 µg/ml), Enterococcus faecalis (MIC=50 µg/ml);
- Gram-negative bacteria: Escherichia coli (MIC=30 µg/ml), Pseudomonas aeruginosa (MIC=50 µg/ml).
- Fungi: Aspergillus niger, Fusarium solani, Fusarium oxysporum.
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Hemolytic Activity
-
- No hemolysis information or data found in the reference(s) presented in this entry
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Cytotoxicity
-
- Not included yet
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Binding Target
- Not found
Structure Information
-
Linear/Cyclic
- Cyclic
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N-terminal Modification
- Free
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C-terminal Modification
- Cyclization(Cys33 and Cys51).
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Nonterminal Modifications and Unusual Amino Acids
- Disulfide bonds between Cys7 and Cys26,Cys14 and Cys40,Cys28 and Cys49,Cys33 and Cys51.
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Stereochemistry
- L
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Structure
- Not found
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Structure Description
- Not found
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Helical Wheel Diagram
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PDB ID
- None
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Predicted Structure
- Please click DRAMP03280_predicted_structure.pdb to download.
Physicochemical Information
-
Formula
- C250H393N67O74S8
Absent Amino Acids
- HLMW
Common Amino Acids
- K
Mass
- 5777.76
PI
- 9.06
Basic Residues
- 12
Acidic Residues
- 5
Hydrophobic Residues
- 9
Net Charge
- +7
-
Boman Index
- -100.48
Hydrophobicity
- -0.755
Aliphatic Index
- 34.51
Half Life
-
- Mammalian:4.4 hour
- Yeast:>20 hour
- E.coli:>10 hour
Extinction Coefficient Cystines
- 9440
Absorbance 280nm
- 188.8
Polar Residues
- 23
DRAMP03280
Comments Information
This basic, Cys-rich antifungal peptide is also active against bacteria. AcAMP was sensitive to proteolytic enzymes, stable between pH 5.0 and 10.0, and heat resistant (15 min at 100 degrees C).
Literature Information
- ·Literature 1
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Title
- A highly thermostable antimicrobial peptide from Aspergillus clavatus ES1: biochemical and molecular characterization.
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Pubmed ID
- 20440534
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Reference
- J Ind Microbiol Biotechnol. 2010 Aug;37(8):805-813.
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Author
- Hajji M, Jellouli K, Hmidet N, Balti R, Sellami-Kamoun A, Nasri M.